Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase.

@article{Bastidas2012RoleON,
  title={Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase.},
  author={Adam C. Bastidas and Michael S. Deal and Jon M. Steichen and Malik M. Keshwani and Yurong Guo and Susan S. Taylor},
  journal={Journal of molecular biology},
  year={2012},
  volume={422 2},
  pages={
          215-29
        }
}
The catalytic (C) subunit of cAMP-dependent protein kinase [protein kinase A (PKA)] is a major target of cAMP signaling, and its regulation is of fundamental importance to biological processes. One mode of regulation is N-myristylation, which has eluded structural and functional characterization so far because most crystal structures are of the non-myristylated enzyme, are phosphorylated on Ser10, and generally lack electron density for the first 13 residues. We crystallized myristylated wild… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 1 time. VIEW TWEETS

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

An Isoform-Specific Myristylation Switch Targets Type II PKA Holoenzymes to Membranes.

Structure • 2015
View 15 Excerpts
Method Support
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 61 references

Comparative surface geometry of the protein kinase family.

Protein science : a publication of the Protein Society • 2009
View 7 Excerpts
Highly Influenced

Contribution of non-catalytic core residues to activity and regulation in protein kinase A.

The Journal of biological chemistry • 2009
View 7 Excerpts
Highly Influenced

Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism.

Proceedings of the National Academy of Sciences of the United States of America • 2006
View 8 Excerpts
Highly Influenced

A-kinase-interacting protein localizes protein kinase A in the nucleus.

Proceedings of the National Academy of Sciences of the United States of America • 2005
View 3 Excerpts
Highly Influenced

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26 Å: new insights into the catalytic mechanism

J. Yang, L. F. Ten Eyck, N. H. Xuong, S. S. Taylor
J. Mol. Biol • 2004
View 8 Excerpts
Highly Influenced